Abstract
Molecular dynamics of PrP 180–193 has allowed us to investigate the stability of the α-helical conformation of the zwitterionic peptide (L 1) and the neutralized (L 2). In water, the helical structure of L 1 is unstable; in L 2, the α-helix breaks up in the middle at Gln186, and the two resulting connected helices are stable. The hydrophobic enviroment decreases the stability of the helical structure of L 1, this effect is more evident for L 2 for which the unfolding of the C-terminus is followed by the formation of an intramolecular hydrogen bond connecting His 187 with Thr 191.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
